2f2q
From Proteopedia
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|PDB= 2f2q |SIZE=350|CAPTION= <scene name='initialview01'>2f2q</scene>, resolution 1.45Å | |PDB= 2f2q |SIZE=350|CAPTION= <scene name='initialview01'>2f2q</scene>, resolution 1.45Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GAI:GUANIDINE'>GAI</scene> | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GAI:GUANIDINE'>GAI</scene>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span> |
| - | |GENE= E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | + | |GENE= E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 Enterobacteria phage T4]) |
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f2q OCA], [http://www.ebi.ac.uk/pdbsum/2f2q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f2q RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2F2Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 2F2Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F2Q OCA]. |
==Reference== | ==Reference== | ||
Guanidinium derivatives bind preferentially and trigger long-distance conformational changes in an engineered T4 lysozyme., Yousef MS, Bischoff N, Dyer CM, Baase WA, Matthews BW, Protein Sci. 2006 Apr;15(4):853-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16600969 16600969] | Guanidinium derivatives bind preferentially and trigger long-distance conformational changes in an engineered T4 lysozyme., Yousef MS, Bischoff N, Dyer CM, Baase WA, Matthews BW, Protein Sci. 2006 Apr;15(4):853-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16600969 16600969] | ||
| - | [[Category: | + | [[Category: Enterobacteria phage t4]] |
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Matthews, B W.]] | [[Category: Matthews, B W.]] | ||
[[Category: Yousef, M S.]] | [[Category: Yousef, M S.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: GAI]] | ||
| - | [[Category: HED]] | ||
[[Category: molecular switch]] | [[Category: molecular switch]] | ||
[[Category: nano-bitechnology]] | [[Category: nano-bitechnology]] | ||
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[[Category: t4 lysozyme]] | [[Category: t4 lysozyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:57:08 2008'' |
Revision as of 23:57, 30 March 2008
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| , resolution 1.45Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | E (Enterobacteria phage T4) | ||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
High resolution crystal strcuture of T4 lysosyme mutant L20R63/A liganded to guanidinium ion
Overview
The binding of guanidinium ion has been shown to promote a large-scale translation of a tandemly duplicated helix in an engineered mutant of T4 lysozyme. The guanidinium ion acts as a surrogate for the guanidino group of an arginine side chain. Here we determine whether methyl- and ethylguanidinium provide better mimics. The results show that addition of the hydrophobic moieties to the ligand enhances the binding affinity concomitant with reduction in ligand solubility. Crystallographic analysis confirms that binding of the alternative ligands to the engineered site still drives the large-scale conformational change. Thermal analysis and NMR data show, in comparison to guanidinium, an increase in protein stability and in ligand affinity. This is presumably due to the successive increase in hydrophobicity in going from guanidinium to ethylguanidinium. A fluorescence-based optical method was developed to sense the ligand-triggered helix translation in solution. The results are a first step in the de novo design of a molecular switch that is not related to the normal function of the protein.
About this Structure
2F2Q is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.
Reference
Guanidinium derivatives bind preferentially and trigger long-distance conformational changes in an engineered T4 lysozyme., Yousef MS, Bischoff N, Dyer CM, Baase WA, Matthews BW, Protein Sci. 2006 Apr;15(4):853-61. PMID:16600969
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